Findings on the interaction of the antimicrobial peptide cecropin-melittin with a gold surface from molecular dynamics studies

The immobilization of gold nanoparticles (AuNPs) with antimicrobial peptides (AMPs) is a new and promising way to enhance both the activity and targeting capabilities of AMPs. However, a full understanding of the adsorption process underlying these materials is still lacking. Cecropin-melittin is a...

Full description

Saved in:
Bibliographic Details
Published in:European biophysics journal 2017-04, Vol.46 (3), p.247-256
Main Authors: Ferreira, André F., Rai, Akhilesh, Ferreira, Lino, Simões, Pedro N.
Format: Article
Language:English
Subjects:
Adsorption
Amino Acid Sequence
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Cecropins - chemistry
Cell Biology
Gold
Gold - chemistry
Life Sciences
Melitten - chemistry
Membrane Biology
Metal Nanoparticles - chemistry
Molecular Dynamics Simulation
Molecular physics
Nanoparticles
Nanotechnology
Neurobiology
Original Article
Peptides
Protein Binding
Protein Conformation
Simulation
Surface Properties
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The immobilization of gold nanoparticles (AuNPs) with antimicrobial peptides (AMPs) is a new and promising way to enhance both the activity and targeting capabilities of AMPs. However, a full understanding of the adsorption process underlying these materials is still lacking. Cecropin-melittin is a peptide with a broad antimicrobial activity while displaying low hemolytic properties, whose conjugation with AuNPs has not been studied before. In this context, we report the investigation of the adsorption process of the cecropin-melittin peptide, with (CM-SH) and without (CM) cysteine at its C-terminus, onto a gold surface based on all-atom MD simulations. Our results show that the way the peptides approach the surface dictates the final conformation and the time required to achieve it in both CM-SH and CM cases. Most important, it is demonstrated that the presence of cysteine promotes a faster conformational stabilization during the lockdown regime of the CM-SH peptide, noticeably affecting this by acting as a preferential anchoring point. This investigation represents a first step in rationalizing, with atomistic detail, some experimentally observed features of CM-SH and CM immobilized gold nanoparticles.
ISSN:0175-7571
1432-1017
DOI:10.1007/s00249-016-1160-z